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W A WOOD

Publications and source records attributed to W A WOOD.

At least 19 recordsLinked to original sources
PubMed1965

METABOLISM OF PENTOSES AND PENTITOLS BY AEROBACTER AEROGENES. 3. PHYSICAL AND IMMUNOLOGICAL PROPERTIES OF PENITOL DEHYDROGENASES AND PENTULOKINASES.

Mortlock, R. P. (Michigan State University, East Lansing), D. D. Fossitt, D. H. Petering, and W. A. Wood. Metabolism of pentoses and pentitols by Aerobacter aerogenes. III. Physical and immunological properties of pentitol dehydrogenases and pentulokinases. J. Bacteriol. 89:129-135. 1965.-Four pentulokinases and three pentitol dehydrogenases were purified from Aerobacter aerogenes PRL-R3, and the properties of the enzymes within each family were compared. d-Ribulokinase was purified from cells grown on ribitol, d-arabitol, and xylitol, and from a mutant constitutive for ribitol dehydrogenase; d-xylulokinase, from cells grown on d-xylose and xylitol; l-ribulokinase, from cells grown on l-arabinose; and l-xylulokinase, after growth on l-xylose. Similarly, ribitol dehydrogenase was purified after growth on ribitol, d-arabinose, and xylitol, and from the ribitol dehydrogenase-constitutive mutant. d-Arabitol dehydrogenase was obtained after growth on d-arabitol or d-xylose, and xylitol dehydrogenase was obtained after growth on xylitol. Except for l-xylulokinase, which also had a different S(20) value, the pentulokinases had identical pH optima, K(m) for the ketopentose, and sedimentation constants, and fractionated identically by a number of procedures. These kinases could be distinguished only by their substrate and immunological specificity. Ribitol dehydrogenase and d-arabitol dehydrogenase could be distinguished by several properties, but the properties of xylitol dehydrogenase were always similar to ribitol dehydrogenase. In all cases, individual kinases or dehydrogenases produced by different inducers had identical properties. These data constitute evidence against multiple forms of the same enzyme being produced by different inducers and against the dehydrogenase family containing essentially identical proteins differing only at the active site. For the kinases, three of the four appear to differ only at the active site.

Antibodies↗
PubMed1965

ENZYMATIC BASIS FOR D-ARBITOL PRODUCTION BY SACCHAROMYCES ROUXII.

Ingram, Jordan M. (Michigan State University, East Lansing), and W. A. Wood. Enzymatic basis for d-arabitol production by Saccharomyces rouxii. J. Bacteriol. 89:1186-1194. 1965.-The enzymatic steps in d-arabitol synthesis by Saccharomyces rouxii were studied. The fermentation of d-glucose-6-C(14) gave rise to d-arabitol labeled at C-5; d-ribose of ribonucleic acid had the same isotope pattern. Crude extracts were able to reduce d-ribulose with reduced nicotinamide adenine dinucleotide phosphate (NADPH(2)) and d-xylulose with reduced nicotinamide adenine dinucleotide (NADH(2)). These extracts also oxidized d-arabitol with nicotinamide adenine dinucleotide phosphate and xylitol with nicotinamide adenine dinucleotide. No reduction of d-ribulose-5-phosphate or d-xylulose-5-phosphate was observed. An enzyme which reduced d-xylulose with NADH(2) was purified 33-fold and characterized as a xylitol (--> d-xylulose) dehydrogenase. Similarly, an enzyme reducing d-ribulose with NADPH(2) was purified 12-fold and characterized as a d-arabitol (--> d-ribulose) dehydrogenase. Alkaline and acid phosphatases were purified 50- and 40-fold, respectively, and their specificities were determined. Only the acid phosphatase had detectable activity on d-ribulose-5-phosphate. The data support the postulate that d-arabitol arises by dephosphorylation of d-ribulose-5-phosphate and reduction of d-ribulose by a NADPH(2)-linked d-arabitol (--> d-ribulose) dehydrogenase.

Acid Phosphatase↗
PubMed1964

METABOLISM OF PENTOSES AND PENTITOLS BY AEROBACTER AEROGENES. I. DEMONSTRATION OF PENTOSE ISOMERASE, PENTULOKINASE, AND PENTITOL DEHYDROGENASE ENZYME FAMILIES.

Mortlock, R. P. (Michigan State University, East Lansing) and W. A. Wood. Metabolism of pentoses and pentitols by Aerobacter aerogenes. I. Demonstration of pentose isomerase, pentulokinase, and pentitol dehydrogenase enzyme families. J. Bacteriol. 88:838-844. 1964.-Aerobacter aerogenes PRL-R3 is capable of utilizing as sole substrates for energy and growth seven of the eight aldopentoses and all of the four pentitols. Growth upon media containing either d-xylose, l-arabinose, d-ribose, d-arabitol, or ribitol occurred within 24 hr at 26 C. When d-arabinose or l-arabitol were used as growth substrates, growth was complete within 2 days; 4 days were required for growth on d-lyxose or xylitol, and 3 to 4 weeks for growth upon l-xylose. The versatility of this strain of A. aerogenes is due to an ability to synthesize in the presence of appropriate carbohydrates (inducers) families of enzymes which catalyze the metabolism of the carbohydrates (i.e., families of pentitol dehydrogenases, aldopentose isomerases, and pentulokinases). The specificity of induction for members of the enzyme families was found to vary, and cross induction of enzyme activity was common, especially among the pentitol dehydrogenases. Ribitol dehydrogenase activity was detected in extracts of cells grown on all of the above carbohydrates with the exception of d-xylose, l-arabinose, and d-ribose. The ribitol dehydrogenase activity of xylitol-grown cell extracts was fivefold higher than the activity in extracts of ribitol-grown cells.

Alcohols↗
PubMed1964

METABOLISM OF PENTOSES AND PENTITOLS BY AEROBACTER AEROGENES. II. MECHANISM OF ACQUISITION OF KINASE, ISOMERASE, AND DEHYDROGENASE ACTIVITY.

Mortlock, R. P. (Michigan State University, East Lansing), and W. A. Wood. Metabolism of pentoses by Aerobacter aerogenes. II. Mechanism of acquisition of kinase, isomerase, and dehydrogenase activity. J. Bacteriol. 88:845-849. 1964.-Aerobacter aerogenes PRL-R3 possesses the genetic information to synthesize, in the presence of the appropriate inducer, at least three members of the family of ketopentokinases, two members of the family of pentitol dehydrogenases, and two members of the family of aldopentose isomerases. That is, d-xylulokinase, d-ribulokinase, l-ribulokinase, ribitol dehydrogenase, d-arabitol dehydrogenase, d-xylose (--> d-xylulose) isomerase, and l-arabinose (--> l-ribulose) isomerase activities were detectable within 4 hr after addition of inducer. The possibility that mutation and selection are involved in the formation of l-xylulokinase, l-arabitol dehydrogenase, d-arabinose (--> d-ribulose) isomerase and d-lyxose (--> d-xylulose) isomerase could not be eliminated, because 11 hr or more of incubation after the addition of inducer were required before the appearance of these enzyme activities. d-Xylulokinase activity was induced in less than 2 hr when d-xylose or d-arabitol were inducers, but 45 hr were required for the appearance of activity when xylitol was the inducer, and 83 hr were required when d-lyxose was the inducer. Likewise, the time required for induction of ribitol dehydrogenase was 2 hr for ribitol, 12 hr for d-arabinose, and 45 hr for xylitol. The time required for the appearance of enzyme activity correlated with the time required for the beginning of cell growth and substrate utilization.

Alcohols↗
PubMed1963

CONVERSION OF GLUCOSE-C14 TO PROPIONATE BY THE RUMEN MICROBIOTA.

Baldwin, R. L. (Michigan State University, East Lansing), W. A. Wood, and R. S. Emery. Conversion of glucose-C(14) to propionate by the rumen microbiota. J. Bacteriol 85:1346-1349. 1963.-Rumen microbiota enriched on three different diets calculated to present different levels of available carbohydrate were incubated with glucose-1-C(14), glucose-2-C(14), and glucose-6-C(14) to determine the contribution of the randomizing (succinate) and nonrandomizing (acrylate) routes to propionate. The propionate was labeled as though 70 to 100% was formed via the randomizing route and 0 to 30% via the nonrandomizing route. The contribution of the acrylate pathway increased with higher carbohydrate availability of the diet. These results are discussed with respect to earlier data using lactate-2-C(14) and lactate-3-C(14), and a unifying concept for both sets of data is presented.

Acrylates↗
PubMed1962

Conversion of lactate-C14 to propionate by the rumen microflora.

Baldwin, R. L. (Michigan State University, East Lansing), W. A. Wood, and R. S. Emery. Conversion of lactate-C(14) to propionate by the rumen microflora. J. Bacteriol. 83:907-913. 1962.-Rumen microflora enriched on five different diets calculated to present increasing carbohydrate or lactate availability were used to determine the contribution of the randomizing (succinate) and nonrandomizing (acrylate) routes to propionate with lactate-2-C(14) and -3-C(14) as substrates. Propionate was labeled as though 70 to 90% was formed via the nonrandomizing route. This percentage was highest on diets containing high levels of carbohydrate or lactate or both. Evidence for the presence of succinic dehydrogenase, acetokinase, phosphotransacetylase, and coenzyme A transphorase was obtained with cell-free extracts. Propionate-2-C(14) and lactate-2-C(14) were converted by extracts to the activated derivatives of acrylate, lactate, propionate, and acetate.

Acetates↗
PubMed1962

Enzyme distribution in membrane, cytoplasm, and nuclear fractions from Pseudomonas fluorescens.

Burrous, S. E. (University of Illinois, Urbana) and W. A. Wood. Enzyme distribution in membrane, cytoplasm, and nuclear fractions from Pseudomonas fluorescens. J. Bacteriol. 84:364-369. 1962.-A procedure is described for fractionation of Pseudomonas fluorescens A3.12 by controlled rupture of spheroplasts and fractional centrifugations to yield cytoplasm, membrane, and deoxyribonucleic acid (DNA) fractions with low cross contamination and little loss of enzymatic activity. Assays for the content of a number of oxidative and nonoxidative enzymes revealed that: (i) little activity is present in the DNA fraction; (ii) only reduced diphosphopyridine nucleotide oxidase is found exclusively in the membranes; (iii) phosphohexosisomerase and probably transketolase and glucose-6-phosphate dehydrogenase are found exclusively in the cytoplasm; and (iv) the remaining five enzymes studied were found in both fractions. In contrast to earlier reports of gluconic dehydrogenase being membrane-bound and 2-keto-3-deoxy-6-phosphogluconate aldolase being soluble in sonic extracts, this procedure produced partly soluble gluconic dehydrogenase and partly membrane-associated 2-keto-3-deoxy-6-phosphogluconate aldolase.

Aldehyde-Lyases↗